2cfp
From Proteopedia
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|PDB= 2cfp |SIZE=350|CAPTION= <scene name='initialview01'>2cfp</scene>, resolution 3.30Å | |PDB= 2cfp |SIZE=350|CAPTION= <scene name='initialview01'>2cfp</scene>, resolution 3.30Å | ||
|SITE= <scene name='pdbsite=AC2:Hg+Binding+Site+For+Chain+A'>AC2</scene> | |SITE= <scene name='pdbsite=AC2:Hg+Binding+Site+For+Chain+A'>AC2</scene> | ||
| - | |LIGAND= <scene name='pdbligand=HG:MERCURY (II) ION'>HG</scene> | + | |LIGAND= <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cfp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cfp OCA], [http://www.ebi.ac.uk/pdbsum/2cfp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2cfp RCSB]</span> | ||
}} | }} | ||
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[[Category: Mirza, O.]] | [[Category: Mirza, O.]] | ||
[[Category: Verner, G.]] | [[Category: Verner, G.]] | ||
| - | [[Category: HG]] | ||
[[Category: formylation]] | [[Category: formylation]] | ||
[[Category: lactose permease]] | [[Category: lactose permease]] | ||
| Line 35: | Line 37: | ||
[[Category: transport mechanism]] | [[Category: transport mechanism]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:20:48 2008'' |
Revision as of 23:20, 30 March 2008
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| , resolution 3.30Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SUGAR FREE LACTOSE PERMEASE AT ACIDIC PH
Overview
Cation-coupled active transport is an essential cellular process found ubiquitously in all living organisms. Here, we present two novel ligand-free X-ray structures of the lactose permease (LacY) of Escherichia coli determined at acidic and neutral pH, and propose a model for the mechanism of coupling between lactose and H+ translocation. No sugar-binding site is observed in the absence of ligand, and deprotonation of the key residue Glu269 is associated with ligand binding. Thus, substrate induces formation of the sugar-binding site, as well as the initial step in H+ transduction.
About this Structure
2CFP is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structural evidence for induced fit and a mechanism for sugar/H+ symport in LacY., Mirza O, Guan L, Verner G, Iwata S, Kaback HR, EMBO J. 2006 Mar 22;25(6):1177-83. Epub 2006 Mar 9. PMID:16525509
Page seeded by OCA on Mon Mar 31 02:20:48 2008
